We are examining the folding dynamics of GCN-4 dimeric peptide using single molecule fluorescence microscopy. The N-terminus of each monomer is tagged with a different fluorescent dye. The two dyes, Texas Red and Rhodamine 6G form a Forster energy transfer pair which is sensitive to the conformational state of GCN-4. The observed fluorescence of the dye system becomes a direct monitor of the conformational state of the peptide. We have observed distinct correlations of fluorescence intensity fluctuations for each dye in the pair which correspond to these structural fluctuations. Methods are being developed to obtain the potential surfaces for the folded and unfolded states in GCN-4 (see Highlights).